Journal of Bacteriology最新文献

{"title":"Pulcherriminic acid as an antibiofilm effector: expanding <i>Bacillus</i> functionality against yeast biofilms.","authors":"Ramya Srinivasan, Tamil Selvam Saravanan, Soham Utpat, Moshe Shemesh, Satish Kumar Rajasekharan","doi":"10.1128/jb.00184-26","DOIUrl":"10.1128/jb.00184-26","url":null,"abstract":"<p><p>Pathogenic and persistent biofilms are a major challenge in medicine and industry, acting as resilient microbial communities that resist antibiotics and cause persistent infections. In this review, we discuss pulcherriminic acid, a promising iron-chelating molecule produced by antagonistic <i>Bacillus subtilis</i> as a natural weapon against persistent biofilms, particularly those formed by pathogens such as <i>Candida albicans</i>. Drawing on recent research, we explore pulcherriminic acid biosynthesis, its native mechanism of depriving fungi of essential iron to disrupt their growth and virulence, and innovative methods to enhance its production through metabolic engineering. We also highlight its potential applications, from fighting infections to serving as a biocontrol agent in agriculture and even as a natural preservative in food. By harnessing this <i>Bacillus</i>-derived metabolite, we suggest sustainable ideas for tackling antibiotic resistance and persistent biofilm-related problems.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0018426"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584742/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148678786","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"FlgJ cell-wall hydrolyzing activity enhances, but is not required, for flagellum assembly in <i>Salmonella enterica</i>.","authors":"Yann H U Chevance, Miki Kinoshita, Fabienne F V Chevance, Tohru Minamino, Keiichi Namba, Kelly T Hughes","doi":"10.1128/jb.00238-26","DOIUrl":"10.1128/jb.00238-26","url":null,"abstract":"<p><p>Penetration of the peptidoglycan (PG) layer by the nascent flagellar rod is a critical step in basal body assembly and has long been attributed to the acetylglucosaminidase activity of the flagellar rod cap protein FlgJ. Previous work in <i>Salmonella enterica</i> suggested that occasional preexisting openings in the PG layer allow some flagella to assemble in the absence of the FlgJ enzymatic activity. More recently, studies in <i>Bacillus subtilis</i> demonstrated that membrane mobility of nascent flagellar structures enables rod penetration without dedicated PG hydrolysis. Here, we revisited the requirement for FlgJ acetylglucosaminidase activity in <i>S. enterica</i> by testing whether inhibition of class 3 flagellar gene expression by the anti-σ28 factor FlgM contributes to the flagellation defect of FlgJ catalytic mutants. Consistent with previous studies, loss of FlgJ acetylglucosaminidase activity did not abolish flagellar assembly but instead reduced its efficiency, resulting in a heterogeneous population in which many cells assembled functional basal bodies and flagella. Deletion of <i>flgM</i> significantly increased both the proportion of flagellated cells and the number of flagellar filaments per cell, indicating that reduced class three gene expression contributes substantially to the observed defect. These findings support a model in which FlgJ enzymatic activity enhances the efficiency of local PG remodeling but is not essential for rod penetration or basal body assembly. Our results demonstrate that acetylglucosaminidase-independent flagellar rod growth occurs in <i>S. enterica</i>, although less efficiently than in organisms that lack FlgJ-like PG hydrolases, highlighting the evolutionary diversity of mechanisms that accommodate flagellar assembly through the bacterial cell wall.IMPORTANCEBacterial flagella allow pathogens, such as <i>Salmonella</i>, to navigate complex environments and invade host cells. During flagellar assembly, the basal body must traverse the peptidoglycan layer, a step-long thought to require the dedicated cell wall-degrading activity of FlgJ. Here, we show that <i>Salmonella</i> can assemble functional flagella, even when the acetylglucosaminidase activity of FlgJ is genetically inactivated. Although these mutants produce fewer flagella per cell, the assembly pathway remains active, and enhanced σ²⁸-dependent gene expression partially restores flagellation. These findings reveal that early steps in flagellar assembly are more diverse than previously thought and that differences in cell wall structure between gram-positive and -negative bacteria likely determine whether a cell wall hydrolyzing activity is required for flagellum assembly.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0023826"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584718/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148793181","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Functional diversity of accessory factors of the type VI secretion system.","authors":"Casey Latario, Benjamin D Ross","doi":"10.1128/jb.00211-26","DOIUrl":"10.1128/jb.00211-26","url":null,"abstract":"<p><p>The type VI secretion system (T6SS) is a nanomachine utilized by Gram-negative bacteria to secrete toxic effectors. The T6SS is employed against both prokaryotic and eukaryotic targets, allowing for competitive advantage and virulence of the attackers in a wide variety of environments. Recent work has revealed the great diversity of T6SS systems. Beyond the canonical, conserved architectural genes of the T6SS, diverse T6SS-associated genes (TAGs) are employed to optimize T6SS activity, compensate for variations in architecture, and dictate T6SS use. Although various TAGs have been discovered in T6SS gene clusters, they display unique activities in modifying their cognate T6SS. In this review, we discuss several of the better-studied TAGs, as well as highlight under-researched TAGs that are likely of great significance. As a means to better understand TAG roles, identify common principles and unifying themes, we present the following six functional categories: Firing Coordinators, Target Recognition Factors, Structural Factors, Transcriptional Regulators, Secretion Regulators, and Unknown TAGs.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0021126"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584744/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148793500","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Monounsaturated fatty acid biosynthesis is critical for streptococcal envelope homeostasis and stress tolerance.","authors":"Jonathon L Baker, Jonah Tang, Mingzhe Guo, Felipe Fabrício Farias-da-Silva, Matthew Barbisan, Molly Burnside, Kaitlin Crofton, Samantha Williams, Saarin Rao, Michelle Lee, Sadie G Drucker, Daniel Kim, Dustin Higashi, Justin Merritt, Yujiro Hirose, Jan-Willem Veening, Victor Nizet","doi":"10.1128/jb.00026-26","DOIUrl":"10.1128/jb.00026-26","url":null,"abstract":"<p><p>The genus <i>Streptococcus</i> contains some of the most important commensals and pathogens of the human microbiome. To obtain the fatty acids required for cell membranes, <i>Streptococcus</i> either produce fatty acids <i>de novo</i> through the fatty acid biosynthesis (<i>fab</i>) pathway or uptake host fatty acids through the fatty acid kinase (<i>fak</i>) pathway. Although both the <i>fab</i> and <i>fak</i> pathways represent potential therapeutic targets to prevent or treat infection<i>,</i> progress is limited because of an incomplete understanding of taxon-to-taxon variability in streptococcal lipid metabolism. Here, we examined the role of <i>de novo</i> monounsaturated fatty acid (MUFA) synthesis in physiology and virulence-associated traits in <i>Streptococcus mutans, Streptococcus pyogenes,</i> and <i>Streptococcus pneumoniae,</i> three major pathogens that cause disease at distinct body sites. In all three species, deletion of <i>fabM</i> abolished MUFA production and caused severe growth defects, decreased stress tolerance, increased antibiotic susceptibility, and defects in cell viability, morphology, and division. In <i>S. mutans,</i> loss of <i>fabM</i> also markedly reduced competence signaling and production of the mutacin IV bacteriocin. Deletion of <i>fabM</i> increased susceptibility to killing by human neutrophils in <i>S. mutans</i> and <i>S. pneumoniae,</i> but not <i>S. pyogenes</i>. Together, these findings illustrate that MUFA synthesis is broadly important for streptococcal physiology and cell membrane homeostasis, while its contribution to pathogenesis is strongly species- and context-dependent, providing leads to guide the development of novel therapeutic and/or preventative strategies.IMPORTANCE<i>Streptococcus</i> spp. exert profound effects on human health, with several species causing significant morbidity and mortality. Although streptococcal fatty acid biosynthesis and utilization are attractive metabolic targets for development of therapeutics, this opportunity is vexed by an incomplete understanding of taxon-to-taxon variability in lipid metabolism. In this study, the role of <i>de novo</i> monounsaturated fatty acid (MUFA) synthesis in physiology and virulence-associated traits was examined in <i>Streptococcus mutans, Streptococcus pyogenes,</i> and <i>Streptococcus pneumoniae,</i> three major pathogens that cause disease at distinct body sites. MUFA synthesis was important for stress and antibiotic tolerance across all three species, while its impact on virulence was species- and context-dependent. Overall, these discoveries provide leads to guide the development of novel therapeutic and/or preventative strategies.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0002626"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584702/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148684546","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Blocked transcription-translation complexes are rescued by transcript release followed by <i>trans</i>-translation.","authors":"Stephanie L Leedom, Kenneth C Keiler","doi":"10.1128/jb.00270-26","DOIUrl":"10.1128/jb.00270-26","url":null,"abstract":"<p><p>Bacterial ribosomes initiate translation while the nascent transcript is still engaged with RNA polymerase, creating a risk that translating ribosomes will become trapped if RNA polymerase is blocked before transcription of the stop codon. Here we show that DNA-binding proteins block RNA polymerase and translating ribosomes <i>in vitro</i> and <i>in vivo</i>. Translating ribosomes are rescued after they trigger the release of the nascent transcript from RNA polymerase. Following the release of the transcript, ribosomes translate to the 3' end of the mRNA and are rescued by <i>trans</i>-translation. This mechanism allows the rescue of all components of blocked transcription-translation reactions.</p><p><strong>Importance: </strong>Co-transcriptional translation in bacteria provides an efficient means to produce proteins but creates a risk that translating ribosomes could become trapped if RNA polymerase is blocked during transcription. We show that when RNA polymerase is blocked, a translating ribosome triggers the release of the nascent mRNA from the polymerase, and the ribosome is rescued by <i>trans</i>-translation. This mechanism for resolving blocked transcription-translation complexes explains how bacteria avoid detrimental accumulation of stalled ribosomes.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0027026"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584721/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148678740","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Loss of the Ap₄A hydrolase YqeK impairs stress adaptation and virulence gene expression in <i>Staphylococcus aureus</i>.","authors":"J Vidaud, J F Coker, J Silva, G S Davidson, C C Anderson, G M Bassett, A A Harry, T Dusenbury, T M Gardner, M L Melear, N J Moraga, J D Fender, C M McMahon, M R Grosser","doi":"10.1128/jb.00265-26","DOIUrl":"10.1128/jb.00265-26","url":null,"abstract":"<p><p>The nucleotide diadenosine tetraphosphate (Ap₄A) accumulates during stress across organisms and cell types and is widely hypothesized to be an alarmone or second messenger. While gram-negative bacteria use ApaH-family hydrolases to degrade Ap₄A and other dinucleoside tetraphosphates (Ap₄Ns), gram-positive bacteria, including <i>Staphylococcus aureus,</i> use YqeK. Inactivation of Ap₄A hydrolases and corresponding Ap₄A accumulation cause diverse phenotypic effects in gram-negative and gram-positive species, ranging from increased antimicrobial sensitivity to reduced virulence. However, the physiological role of YqeK in <i>S. aureus</i> remains uncharacterized. Here, we constructed an isogenic <i>yqeK</i> mutant in <i>S. aureus</i> and showed that ∆<i>yqeK</i> was sensitive to nitrosative and organic acid stress, with all phenotypes restored by complementation. We used a luminescence-based assay to quantify relative Ap₄Ns and found that ∆<i>yqeK</i> had ~1,000 fold higher signal than wild-type even during unstressed growth. Transcriptomics revealed that ∆<i>yqeK</i> exhibited stress-specific dysregulation of translation, nucleotide metabolism, central metabolism, iron acquisition, and stress response genes. In contrast, ∆<i>yqeK</i> had few transcriptional differences relative to the wild-type during unstressed growth despite the large Ap₄N accumulation, suggesting that the effects of Ap₄Ns are contingent on the cellular stress state. Unexpectedly, the <i>agr</i> quorum sensing operon and numerous virulence genes showed reduced expression in ∆<i>yqeK</i>, correlating with reduced hemolytic activity. This represents the first reported link between Ap₄N accumulation and quorum sensing suppression in a gram-positive pathogen. Our data reveal YqeK to be a critical metabolic determinant of <i>S. aureus</i> stress resistance and virulence and position this hydrolase as a promising candidate for anti-virulence drug development.</p><p><strong>Importance: </strong><i>Staphylococcus aureus</i> is a leading cause of antibiotic-resistant bacterial infections worldwide and is resistant to many components of the host immune response. Here, we discovered that deletion of YqeK, an enzyme that degrades a stress-associated nucleotide signaling molecule called Ap₄A, rendered <i>S. aureus</i> more susceptible to infection-relevant stress conditions but had little impact on normal growth. Ap₄Ns accumulated in the <i>yqeK</i> mutant and caused major stress-specific changes in gene expression, including reduced expression of key virulence genes. This correlated with a reduction in the destruction of red blood cells, a measure of bacterial toxicity toward host cells. Our data suggest that YqeK represents a promising target for new drugs aimed at reducing the virulence of <i>S. aureus</i>.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0026526"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584722/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148793464","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The role of extracellular DNA in <i>Neisseria</i> biofilms.","authors":"Jolyn Pan, Adele Williamson","doi":"10.1128/jb.00314-26","DOIUrl":"10.1128/jb.00314-26","url":null,"abstract":"<p><p>The genus <i>Neisseria</i> includes two human pathogens, <i>Neisseria gonorrhoeae</i> and <i>Neisseria meningitidis</i>, in addition to commensal species that also inhabit human and animal hosts. One of the features that occurs during neisserial host colonization is biofilm formation. In other bacteria, biofilm formation enables persistence as well as evasion of the host immune system. Extracellular DNA (eDNA) forms a major component of <i>Neisseria</i> biofilms and contributes to initial steps in their formation, as well as the structure and stability of the biofilm extracellular matrix. Here, we review the potential roles and sources of eDNA in <i>Neisseria</i> biofilms and its relevance to both pathogenic and commensal <i>Neisseria</i> spp. We also highlight the paucity in research on biofilm formation by commensal <i>Neisseria</i> and hope this will stimulate further research on the role of eDNA in nonpathogenic <i>Neisseria</i>.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0031426"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584700/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148678804","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"<i>Sulfolobus acidocaldarius</i>, half a century of archaeal research.","authors":"Marleen van Wolferen, Michael Spädt, Shamphavi Sivabalasarma, Sonja-Verena Albers","doi":"10.1128/jb.00322-26","DOIUrl":"10.1128/jb.00322-26","url":null,"abstract":"<p><p>Since its isolation from a Yellowstone hot spring in 1972, <i>Sulfolobus acidocaldarius</i> has become one of the most important model organisms for archaeal biology. Initially studied for its remarkable adaptation to high temperature and low pH, it has evolved into a genetically tractable system that has contributed substantially to our understanding of archaeal physiology, molecular biology, and evolution. Here, we summarize more than 5 decades of research on <i>S. acidocaldarius,</i> highlighting key developments in genetic and microscopy tools and their impact on our understanding of archaeal cell biology. Studies in this organism have improved our understanding of archaeal metabolism, chromosome organization, DNA replication and segregation, cell division, protein glycosylation, biofilm formation, and the assembly and regulation of archaeal surface structures, including archaella and type IV pili. Beyond fundamental biology, <i>S. acidocaldarius</i> has also served as a valuable source of thermostable enzymes and other biomolecules with biotechnological potential. Today, <i>S. acidocaldarius</i> is still one of the main model organisms for archaeal biology. Ongoing advances in genetics, imaging, and structural biology continue to expand its experimental potential, while its phylogenetic position within the Thermoproteota makes it a powerful system for investigating the evolutionary origins of eukaryotic cellular complexity.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0032226"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584746/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148678789","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A journal that grows older and stays young.","authors":"Tao Dong","doi":"10.1128/jb.00340-26","DOIUrl":"10.1128/jb.00340-26","url":null,"abstract":"","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0034026"},"PeriodicalIF":3.8,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13584707/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148761155","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"<i>Aeromonas veronii</i> biotype sobria serine protease activates aerolysin and cleaves EpCAM to breach the epithelial barrier.","authors":"Hidetomo Kobayashi, Soshi Seike, Eizo Takahashi, Keinosuke Okamoto, Hiroyasu Yamanaka","doi":"10.1128/jb.00141-26","DOIUrl":"10.1128/jb.00141-26","url":null,"abstract":"<p><p>Infections by <i>Aeromonas</i> can rapidly progress from mucosal colonization to invasive disease, but how these bacteria efficiently breach epithelial barriers is unclear. Here, we define a coordinated two-component virulence strategy in <i>Aeromonas veronii</i> biotype sobria (<i>A. veronii</i> sobria) involving a secreted serine protease (ASP) and aerolysin. In polarized T84 monolayers, wild-type infection caused rapid transepithelial electrical resistance (TEER) loss and degradation of junctional/adhesion proteins. An ASP-deficient strain exhibited delayed barrier collapse with reduced cleavage of ZO-1/2/3 and EpCAM, and purified ASP restored these effects, indicating ASP is required but alone insufficient for full disruption. A transposon screen identified aerolysin and secretion-related genes as key contributors to junctional damage. Mechanistically, ASP directly converted recombinant pro-aerolysin into a hemolytically active toxin <i>in vitro</i>, linking protease activity to toxin maturation. Functionally, ASP and aerolysin synergized to promote bacterial translocation across epithelial monolayers with marked sequence dependence; pro-aerolysin pretreatment enhanced ASP-mediated degradation of ZO proteins, claudin-7, and EpCAM. ASP further cleaved EpCAM at multiple extracellular sites, compromising adhesion and junctional homeostasis. Together, these findings establish an ASP-aerolysin pathway that couples toxin activation with junctional proteolysis to drive structural epithelial breaches.IMPORTANCE<i>Aeromonas</i> infections can rapidly progress from intestinal colonization to invasive disease, yet the molecular steps enabling epithelial breach are unclear. We show that <i>Aeromonas veronii</i> sobria uses a coordinated two-factor pathway in which <i>Aeromonas</i> serine protease (ASP) both activates the pore-forming toxin aerolysin and directly cleaves key junctional/adhesion proteins, including ZO-1/2/3 and EpCAM. Aerolysin primes cells for enhanced ASP-mediated proteolysis in an order-dependent manner, converting TEER loss into a physical barrier rupture that permits massive bacterial translocation. Targeting ASP-aerolysin cooperation may provide a rational anti-virulence strategy.</p>","PeriodicalId":15107,"journal":{"name":"Journal of Bacteriology","volume":" ","pages":"e0014126"},"PeriodicalIF":3.8,"publicationDate":"2026-08-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13492141/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148421491","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}